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Conserved domains on  [gi|2154868141|ref|WP_229674167|]
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EAL domain-containing protein [Sphingomonas prati]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 4-99 1.12e-37

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 134.90  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:COG5001   577 ALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAeDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQ 656

                          90
                  ....*....|....*..
gi 2154868141  83 GYPFSRAIAAEQVPLIL 99
Cdd:COG5001   657 GYLFSRPLPAEELEALL 673
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 4-99 1.12e-37

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 134.90  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:COG5001   577 ALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAeDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQ 656

                          90
                  ....*....|....*..
gi 2154868141  83 GYPFSRAIAAEQVPLIL 99
Cdd:COG5001   657 GYLFSRPLPAEELEALL 673
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-94 7.64e-37

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 125.74  E-value: 7.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:cd01948   149 ALDDFGTGYSSLSYLKRLPVDYLKIDRSFVRDIEtDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQ 228

                          90
                  ....*....|..
gi 2154868141  83 GYPFSRAIAAEQ 94
Cdd:cd01948   229 GYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 4-94 3.77e-33

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 116.16  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141    4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLAL-ADACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:smart00052 151 ALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQ 230

                           90
                   ....*....|..
gi 2154868141   83 GYPFSRAIAAEQ 94
Cdd:smart00052 231 GYLFSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-89 8.11e-26

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 97.00  E-value: 8.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:pfam00563 149 ALDDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDkDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQ 228


                  ....*..
gi 2154868141  83 GYPFSRA 89
Cdd:pfam00563 229 GYYFSKP 235
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 4-94 4.00e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 90.54  E-value: 4.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASL---VHLKKFPVDTLKIDWSFVLALADacNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDH 80
Cdd:PRK13561  551 ALDDFGMGYAGLrqlQHMKSLPIDVLKIDKMFVDGLPE--DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628

                          90
                  ....*....|....
gi 2154868141  81 GQGYPFSRAIAAEQ 94
Cdd:PRK13561  629 AQGFLFARALPIEI 642
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 4-99 1.12e-37

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 134.90  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:COG5001   577 ALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAeDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQ 656

                          90
                  ....*....|....*..
gi 2154868141  83 GYPFSRAIAAEQVPLIL 99
Cdd:COG5001   657 GYLFSRPLPAEELEALL 673
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-94 7.64e-37

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 125.74  E-value: 7.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:cd01948   149 ALDDFGTGYSSLSYLKRLPVDYLKIDRSFVRDIEtDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQ 228

                          90
                  ....*....|..
gi 2154868141  83 GYPFSRAIAAEQ 94
Cdd:cd01948   229 GYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 4-94 3.77e-33

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 116.16  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141    4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLAL-ADACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:smart00052 151 ALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQ 230

                           90
                   ....*....|..
gi 2154868141   83 GYPFSRAIAAEQ 94
Cdd:smart00052 231 GYLFSRPLPLDD 242
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 4-99 2.79e-31

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 116.42  E-value: 2.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:COG2200   479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIArDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558

                          90
                  ....*....|....*..
gi 2154868141  83 GYPFSRAIAAEQVPLIL 99
Cdd:COG2200   559 GYLFGRPLPLEELEALL 575
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 4-94 5.10e-29

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 109.62  E-value: 5.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:COG4943   421 AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGtDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500

                          90
                  ....*....|..
gi 2154868141  83 GYPFSRAIAAEQ 94
Cdd:COG4943   501 GWLFAKPLPAEE 512
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-89 8.11e-26

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 97.00  E-value: 8.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:pfam00563 149 ALDDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDkDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQ 228


                  ....*..
gi 2154868141  83 GYPFSRA 89
Cdd:pfam00563 229 GYYFSKP 235
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 4-94 4.00e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 90.54  E-value: 4.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASL---VHLKKFPVDTLKIDWSFVLALADacNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDH 80
Cdd:PRK13561  551 ALDDFGMGYAGLrqlQHMKSLPIDVLKIDKMFVDGLPE--DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI 628

                          90
                  ....*....|....
gi 2154868141  81 GQGYPFSRAIAAEQ 94
Cdd:PRK13561  629 AQGFLFARALPIEI 642
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 4-102 7.32e-20

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 84.05  E-value: 7.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVlalaDACNV-----GIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGC 78
Cdd:PRK11359  695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFV----DRCLTekrilALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHC 770

                          90       100
                  ....*....|....*....|....
gi 2154868141  79 DHGQGYPFSRAIAAEQVPLILCSY 102
Cdd:PRK11359  771 RVIQGYFFSRPLPAEEIPGWMSSV 794
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
5-94 1.62e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 83.19  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   5 LDDFGTGYASLVHLKKFPVDTLKIDWSFVLAL-ADACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQG 83
Cdd:PRK10060  559 LDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIhKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQG 638

                          90
                  ....*....|.
gi 2154868141  84 YPFSRAIAAEQ 94
Cdd:PRK10060  639 FLFAKPMPAVA 649
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
4-94 1.21e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 77.72  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALA-DACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDHGQ 82
Cdd:PRK10551  414 AIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGtETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQ 493

                          90
                  ....*....|..
gi 2154868141  83 GYPFSRAIAAEQ 94
Cdd:PRK10551  494 GYWISRPLPLED 505
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 4-91 2.22e-15

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 71.13  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141   4 ALDDFGTGYASL---VHLKKFPVDTLKIDWSFV--LALADAcnvgIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGC 78
Cdd:PRK11829  556 ALDDFGIGYSSLrylNHLKSLPIHMIKLDKSFVknLPEDDA----IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGI 631

                          90
                  ....*....|...
gi 2154868141  79 DHGQGYPFSRAIA 91
Cdd:PRK11829  632 QCGQGFLFSPPLP 644
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 2-97 9.06e-12

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 60.84  E-value: 9.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154868141    2 TTALDDFGTGYASLVHLKKFPVDTLKIDWSFVLALAD-ACNVGIVRAIVNLGKDLGITTVTEGIETYAQADPLHYEGCDH 80
Cdd:PRK09776   989 RVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGnLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDL 1068

                           90
                   ....*....|....*..
gi 2154868141   81 GQGYpfsrAIaAEQVPL 97
Cdd:PRK09776  1069 AYGY----AI-ARPQPL 1080
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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